ArticlePloS one2019
Crystal structure of chloramphenicol-metabolizing enzyme EstDL136 from a metagenome.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Molecular determinants for the association of human hormone-sensitive lipase with lipid droplets.Nature communications · 2025Article
- Crystallization and preliminary X-ray crystallographic studies of AfeH from Acimetobacter sp. DL-2.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Identification, characterization, and distribution of novel amidase geneApplied and environmental microbiology · 2024Article
- Euglena mutabilis exists in a FAB consortium with microbes that enhance cadmium tolerance.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- N-terminal lid swapping contributes to the substrate specificity and activity of thermophilic lipase TrLipE.Frontiers in microbiology · 2023Article
- Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.PloS one · 2023Article
- Strategies for Enzymatic Inactivation of the Veterinary Antibiotic Florfenicol.Antibiotics (Basel, Switzerland) · 2022Article
- Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure.Biomolecules · 2021Article
- Crossroads of Antibiotic Resistance and Biosynthesis.Journal of molecular biology · 2019Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metagenomes often convey novel biological activities and therefore have gained considerable attention for use in biotechnological applications. Recently, metagenome-derived EstDL136 was found to possess chloramphenicol (Cm)-metabolizing features. Sequence analysis showed EstDL136 to be a member of the hormone-sensitive lipase (HSL) family with an Asp-His-Ser catalytic triad and a notable substrate specificity. In this study, we determined the crystal structures of EstDL136 and in a complex with Cm. Consistent with the high sequence similarity, the structure of EstDL136 is homologous to that of the HSL family. The active site of EstDL136 is a relatively shallow pocket that could accommodate Cm as a substrate as opposed to the long acyl chain substrates typical of the HSL family. Mutational analyses further suggested that several residues in the vicinity of the active site play roles in the Cm-binding of EstDL136. These results provide structural and functional insights into a metagenome-derived EstDL136.
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